{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,12]],"date-time":"2026-02-12T14:26:37Z","timestamp":1770906397408,"version":"3.50.1"},"reference-count":258,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2022,3,23]],"date-time":"2022-03-23T00:00:00Z","timestamp":1647993600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.mdpi.com"],"crossmark-restriction":true},"short-container-title":["Cancers"],"abstract":"<jats:p>Lysosomes are cellular organelles that regulate essential biological processes such as cellular homeostasis, development, and aging. They are primarily connected to the degradation\/recycling of cellular macromolecules and participate in cellular trafficking, nutritional signaling, energy metabolism, and immune regulation. Therefore, lysosomes connect cellular metabolism and signaling pathways. Lysosome\u2019s involvement in the critical biological processes has rekindled clinical interest towards this organelle for treating various diseases, including cancer. Recent research advancements have demonstrated that lysosomes also regulate the maintenance and hemostasis of hematopoietic stem cells (HSCs), which play a critical role in the progression of acute myeloid leukemia (AML) and other types of cancer. Lysosomes regulate both HSCs\u2019 metabolic networks and identity transition. AML is a lethal type of blood cancer with a poor prognosis that is particularly associated with aging. Although the genetic landscape of AML has been extensively described, only a few targeted therapies have been produced, warranting the need for further research. This review summarizes the functions and importance of targeting lysosomes in AML, while highlighting the significance of lysosomes in HSCs maintenance.<\/jats:p>","DOI":"10.3390\/cancers14071618","type":"journal-article","created":{"date-parts":[[2022,3,23]],"date-time":"2022-03-23T12:20:25Z","timestamp":1648038025000},"page":"1618","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["RETRACTED: Lysosomes in Stem Cell Quiescence: A Potential Therapeutic Target in Acute Myeloid Leukemia"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9235-6236","authenticated-orcid":false,"given":"Vaibhav","family":"Jain","sequence":"first","affiliation":[{"name":"Abramson Cancer Center, Department of Medicine, 421 Curie Blvd., Philadelphia, PA 19104, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Swaroop","family":"Bose","sequence":"additional","affiliation":[{"name":"Department of Dermatology, Mount Sinai Icahn School of Medicine, New York, NY 10029, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2142-4924","authenticated-orcid":false,"given":"Awadhesh","family":"Arya","sequence":"additional","affiliation":[{"name":"Department of Anesthesiology, Shock, Trauma and Anesthesiology Research Center, University of Maryland School of Medicine, Baltimore, MD 21201, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tasleem","family":"Arif","sequence":"additional","affiliation":[{"name":"Department of Cell, Developmental, and Regenerative Biology, Mount Sinai Icahn School of Medicine, New York, NY 10029, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2022,3,23]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1038\/ncb0905-847","article-title":"The lysosome turns fifty","volume":"7","year":"2005","journal-title":"Nat. Cell Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1083\/jcb.124.6.903","article-title":"Ultrastructural analysis of the autophagic process in yeast: Detection of autophagosomes and their characterization","volume":"124","author":"Baba","year":"1994","journal-title":"J. Cell Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1038\/emboj.2012.32","article-title":"A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB","volume":"31","author":"Settembre","year":"2012","journal-title":"EMBO J."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1126\/science.aan6298","article-title":"Lysosomal metabolomics reveals V-ATPase- and mTOR-dependent regulation of amino acid efflux from lysosomes","volume":"358","author":"Wyant","year":"2017","journal-title":"Science"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1038\/nrd.2017.214","article-title":"Emptying the stores: Lysosomal diseases and therapeutic strategies","volume":"17","author":"Platt","year":"2018","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1111\/tra.12714","article-title":"Lysosomal size matters","volume":"21","author":"Liebscher","year":"2020","journal-title":"Traffic"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1038\/nrm2745","article-title":"Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function","volume":"10","author":"Saftig","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"2758","DOI":"10.1073\/pnas.79.9.2758","article-title":"Identification and characterization of a proton pump on lysosomes by fluorescein-isothiocyanate-dextran fluorescence","volume":"79","author":"Ohkuma","year":"1982","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1146\/annurev-cellbio-111315-125125","article-title":"The Lysosome as a Regulatory Hub","volume":"32","author":"Perera","year":"2016","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.tibs.2020.09.004","article-title":"How Lysosomes Sense, Integrate, and Cope with Stress","volume":"46","author":"Saftig","year":"2021","journal-title":"Trends Biochem. Sci."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1016\/j.tcb.2017.07.006","article-title":"Emerging Roles for the Lysosome in Lipid Metabolism","volume":"27","author":"Thelen","year":"2017","journal-title":"Trends Cell Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/s41580-019-0185-4","article-title":"Lysosomes as dynamic regulators of cell and organismal homeostasis","volume":"21","author":"Ballabio","year":"2020","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1016\/j.cell.2017.09.046","article-title":"mTORC1 Activator SLC38A9 Is Required to Efflux Essential Amino Acids from Lysosomes and Use Protein as a Nutrient","volume":"171","author":"Wyant","year":"2017","journal-title":"Cell"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"4329","DOI":"10.1242\/jcs.196287","article-title":"Mechanisms and functions of lysosome positioning","volume":"129","author":"Pu","year":"2016","journal-title":"J. Cell Sci."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/ncb2204","article-title":"Lysosomal positioning coordinates cellular nutrient responses","volume":"13","author":"Korolchuk","year":"2011","journal-title":"Nat. Cell Biol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"4217","DOI":"10.1083\/jcb.201611073","article-title":"PtdIns3P controls mTORC1 signaling through lysosomal positioning","volume":"216","author":"Hong","year":"2017","journal-title":"J. Cell Biol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.molcel.2019.05.009","article-title":"Lysosome Positioning Influences mTORC2 and AKT Signaling","volume":"75","author":"Jia","year":"2019","journal-title":"Mol. Cell"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.cell.2018.05.009","article-title":"Acid Suspends the Circadian Clock in Hypoxia through Inhibition of mTOR","volume":"174","author":"Walton","year":"2018","journal-title":"Cell"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"823","DOI":"10.15252\/embr.201541382","article-title":"Folliculin directs the formation of a Rab34\u2013RILP complex to control the nutrient-dependent dynamic distribution of lysosomes","volume":"17","author":"Starling","year":"2016","journal-title":"EMBO Rep."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1083\/jcb.201507112","article-title":"The position of lysosomes within the cell determines their luminal pH","volume":"212","author":"Johnson","year":"2016","journal-title":"J. Cell Biol."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Buratta, S., Tancini, B., Sagini, K., Delo, F., Chiaradia, E., Urbanelli, L., and Emiliani, C. (2020). Lysosomal Exocytosis, Exosome Release and Secretory Autophagy: The Autophagic- and Endo-Lysosomal Systems Go Extracellular. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21072576"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1038\/ncb839","article-title":"TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling","volume":"4","author":"Inoki","year":"2002","journal-title":"Nat. Cell Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1042\/BST0370289","article-title":"Rag proteins regulate amino-acid-induced mTORC1 signalling","volume":"37","author":"Sancak","year":"2009","journal-title":"Biochem. Soc. Trans."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1038\/s41467-017-01567-4","article-title":"Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1","volume":"8","author":"Zhang","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.1126\/science.1232044","article-title":"A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1","volume":"340","author":"Chantranupong","year":"2013","journal-title":"Science"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1038\/s41580-019-0199-y","article-title":"mTOR at the nexus of nutrition, growth, ageing and disease","volume":"21","author":"Liu","year":"2020","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2297","DOI":"10.1080\/15548627.2020.1831217","article-title":"CDKN1B\/p27 regulates autophagy via the control of Ragulator and MTOR activity in amino acid-deprived cells","volume":"16","author":"Nowosad","year":"2020","journal-title":"Autophagy"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1038\/nature14107","article-title":"SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1","volume":"519","author":"Rebsamen","year":"2015","journal-title":"Nature"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1080\/15548627.2015.1091143","article-title":"SLC38A9: A lysosomal amino acid transporter at the core of the amino acid-sensing machinery that controls MTORC1","volume":"12","author":"Rebsamen","year":"2016","journal-title":"Autophagy"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1126\/science.1207056","article-title":"mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H+-ATPase","volume":"334","author":"Zoncu","year":"2011","journal-title":"Science"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"2479","DOI":"10.1128\/MCB.00125-15","article-title":"Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9","volume":"35","author":"Jung","year":"2015","journal-title":"Mol. Cell. Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1126\/science.1257132","article-title":"Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1","volume":"347","author":"Wang","year":"2015","journal-title":"Science"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1083\/jcb.201307084","article-title":"Recruitment of folliculin to lysosomes supports the amino acid\u2013dependent activation of Rag GTPases","volume":"202","author":"Petit","year":"2013","journal-title":"J. Cell Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/j.molcel.2013.09.016","article-title":"The folliculin tumor suppressor is a GAP for the RagC\/D GTPases that signal amino acid levels to mTORC1","volume":"52","author":"Tsun","year":"2013","journal-title":"Mol. Cell"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1126\/science.aay0166","article-title":"Structural basis for the docking of mTORC1 on the lysosomal surface","volume":"366","author":"Rogala","year":"2019","journal-title":"Science"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1038\/nrm3522","article-title":"Amino acid signalling upstream of mTOR","volume":"14","author":"Jewell","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1496","DOI":"10.1126\/science.1157535","article-title":"The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1","volume":"320","author":"Sancak","year":"2008","journal-title":"Science"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1016\/j.cell.2012.07.032","article-title":"Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1","volume":"150","author":"Schweitzer","year":"2012","journal-title":"Cell"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.molcel.2013.01.024","article-title":"ZKSCAN3 is a master transcriptional repressor of autophagy","volume":"50","author":"Chauhan","year":"2013","journal-title":"Mol. Cell"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2759","DOI":"10.1038\/s41375-021-01388-x","article-title":"Lysosomes in acute myeloid leukemia: Potential therapeutic targets?","volume":"35","author":"Rafiq","year":"2021","journal-title":"Leukemia"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1038\/ncb3114","article-title":"Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB","volume":"17","author":"Medina","year":"2015","journal-title":"Nat. Cell Biol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1007\/s13238-018-0523-x","article-title":"Release and uptake mechanisms of vesicular Ca2+ stores","volume":"10","author":"Yang","year":"2019","journal-title":"Protein Cell"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1242\/jcs.115.3.599","article-title":"pH-dependent regulation of lysosomal calcium in macrophages","volume":"115","author":"Christensen","year":"2002","journal-title":"J. Cell Sci."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"e15887","DOI":"10.7554\/eLife.15887","article-title":"The endoplasmic reticulum, not the pH gradient, drives calcium refilling of lysosomes","volume":"5","author":"Garrity","year":"2016","journal-title":"eLife"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1042\/BJ20110949","article-title":"Molecular mechanisms of endolysosomal Ca2+ signalling in health and disease","volume":"439","author":"Morgan","year":"2011","journal-title":"Biochem. J."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1038\/nrm2217","article-title":"Lysosomes: Fusion and function","volume":"8","author":"Luzio","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1038\/ncb3324","article-title":"A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation","volume":"18","author":"Li","year":"2016","journal-title":"Nat. Cell Biol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"21165","DOI":"10.1073\/pnas.1311864110","article-title":"Genetically encoded fluorescent probe to visualize intracellular phosphatidylinositol 3,5-bisphosphate localization and dynamics","volume":"110","author":"Li","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1038\/nrm.2015.8","article-title":"Structure and function of ER membrane contact sites with other organelles","volume":"17","author":"Phillips","year":"2016","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1146\/annurev-physiol-021014-071649","article-title":"Lysosomal Physiology","volume":"77","author":"Xu","year":"2015","journal-title":"Annu. Rev. Physiol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1083\/jcb.201612123","article-title":"A voltage-dependent K+ channel in the lysosome is required for refilling lysosomal Ca2+ stores","volume":"216","author":"Wang","year":"2017","journal-title":"J. Cell Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1126\/science.aao1583","article-title":"Crystal structure of the human lysosomal mTORC1 scaffold complex and its impact on signaling","volume":"358","author":"Naschberger","year":"2017","journal-title":"Science"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1038\/s41467-017-01762-3","article-title":"Structural basis for the assembly of the Ragulator-Rag GTPase complex","volume":"8","author":"Yonehara","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1515\/bchm3.1995.376.4.225","article-title":"Regulation of the Activity of Lysosomal Cysteine Proteinases by pH-Induced Inactivation and\/or Endogenous Protein Inhibitors, Cystatins","volume":"376","author":"Turk","year":"1995","journal-title":"Biol. Chem. Hoppe-Seyler"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1021\/bi00052a046","article-title":"Kinetics of the pH-induced inactivation of Human cathepsin L.","volume":"32","author":"Turk","year":"1993","journal-title":"Biochemistry"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/S0167-4838(99)00263-0","article-title":"Lysosomal cysteine proteases: More than scavengers","volume":"1477","author":"Turk","year":"2000","journal-title":"Biochim. Biophys. Acta (BBA)-Protein Struct. Mol. Enzym."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1172\/JCI200317740","article-title":"Cathepsin B inactivation attenuates hepatic injury and fibrosis during cholestasis","volume":"112","author":"Canbay","year":"2003","journal-title":"J. Clin. Investig."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1172\/JCI4765","article-title":"Toxic bile salts induce rodent hepatocyte apoptosis via direct activation of Fas","volume":"103","author":"Faubion","year":"1999","journal-title":"J. Clin. Investig."},{"key":"ref_59","first-page":"G723","article-title":"Cystatin A expression reduces bile salt-induced apoptosis in a rat hepatoma cell line","volume":"275","author":"Jones","year":"1998","journal-title":"Am. J. Physiol. Liver Physiol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1714","DOI":"10.1053\/gast.1997.v113.pm9352877","article-title":"Cathepsin B contributes to bile salt-induced apoptosis of rat hepatocytes","volume":"113","author":"Roberts","year":"1997","journal-title":"Gastroenterology"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"2177","DOI":"10.1038\/sj.onc.1201755","article-title":"Potential role for cathepsin D in p53-dependent tumor suppression and chemosensitivity","volume":"16","author":"Wu","year":"1998","journal-title":"Oncogene"},{"key":"ref_62","first-page":"2878","article-title":"Caspase-3 activation by lysosomal enzymes in cytochrome c-independent apoptosis in myelodysplastic syndrome-derived cell line P39","volume":"61","author":"Hishita","year":"2001","journal-title":"Cancer Res."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1807","DOI":"10.1016\/S0002-9440(10)61127-3","article-title":"The lysosomal protease cathepsin l is an important regulator of keratinocyte and melanocyte differentiation during hair follicle morphogenesis and cycling","volume":"160","author":"Tobin","year":"2002","journal-title":"Am. J. Pathol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"7381","DOI":"10.1021\/bi027307q","article-title":"Hurpin is a selective inhibitor of Lysosomal cathepsin L and protects keratinocytes from ultraviolet-induced apoptosis","volume":"42","author":"Welss","year":"2003","journal-title":"Biochemistry"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1515\/BC.2002.112","article-title":"Apoptotic pathways: Involvement of lysosomal proteases","volume":"383","author":"Turk","year":"2002","journal-title":"Biol. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1146\/annurev.physiol.59.1.63","article-title":"Emerging roles for cysteine proteases in human biology","volume":"59","author":"Chapman","year":"1997","journal-title":"Annu. Rev. Physiol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"39499","DOI":"10.1074\/jbc.M206669200","article-title":"Cathepsin B mediates tumor necrosis factor-induced arachidonic acid release in tumor cells","volume":"277","author":"Foghsgaard","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Yadati, T., Houben, T., Bitorina, A., and Shiri-Sverdlov, R. (2020). The Ins and Outs of Cathepsins: Physiological Function and Role in Disease Management. Cells, 9.","DOI":"10.3390\/cells9071679"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1905","DOI":"10.1242\/jcs.091181","article-title":"Lysosomal cell death at a glance","volume":"126","author":"Aits","year":"2013","journal-title":"J. Cell Sci."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1016\/j.bbamcr.2008.09.008","article-title":"Lysosomal involvement in cell death and cancer","volume":"1793","author":"Kirkegaard","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1093\/intimm\/dxy016","article-title":"Mechanisms controlling nucleic acid-sensing Toll-like receptors","volume":"30","author":"Miyake","year":"2018","journal-title":"Int. Immunol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1080\/15548627.2019.1603547","article-title":"Emerging views of mitophagy in immunity and autoimmune diseases","volume":"16","author":"Xu","year":"2020","journal-title":"Autophagy"},{"key":"ref_73","first-page":"301","article-title":"The Transcription Factor EB Links Cellular Stress to the Immune Response","volume":"90","author":"Nabar","year":"2017","journal-title":"Yale J. Biol. Med."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.3389\/fimmu.2018.01643","article-title":"Current Concepts of Antigen Cross-Presentation","volume":"9","author":"Embgenbroich","year":"2018","journal-title":"Front. Immunol."},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Wang, F., Tasset, I., Cuervo, A.M., and Muller, S. (2020). In Vivo Remodeling of Altered Autophagy-Lysosomal Pathway by a Phosphopeptide in Lupus. Cells, 9.","DOI":"10.3390\/cells9102328"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1038\/nature07383","article-title":"Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1\u03b2 production","volume":"456","author":"Saitoh","year":"2008","journal-title":"Nature"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1038\/ni.2215","article-title":"Activation of autophagy by inflammatory signals limits IL-1\u03b2 production by targeting ubiquitinated inflammasomes for destruction","volume":"13","author":"Shi","year":"2012","journal-title":"Nat. Immunol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1080\/15548627.2018.1505155","article-title":"Galectins control MTOR and AMPK in response to lysosomal damage to induce autophagy","volume":"15","author":"Jia","year":"2018","journal-title":"Autophagy"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/S0304-4165(02)00310-0","article-title":"Galectinomics: Finding themes in complexity","volume":"1572","author":"Cooper","year":"2002","journal-title":"Biochim. Biophys. Acta (BBA)-Gen. Subj."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"e17","DOI":"10.1017\/S1462399408000719","article-title":"Galectins: Structure, function and therapeutic potential","volume":"10","author":"Yang","year":"2008","journal-title":"Expert Rev. Mol. Med."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.jbior.2018.09.003","article-title":"Galectins as regulators of cell survival in the leukemia niche","volume":"71","author":"Ruvolo","year":"2018","journal-title":"Adv. Biol. Regul."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1038\/s41421-020-0141-7","article-title":"Lysosome biology in autophagy","volume":"6","author":"Yim","year":"2020","journal-title":"Cell Discov."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1016\/j.devcel.2021.02.002","article-title":"Autophagosome maturation stymied by SARS-CoV-2","volume":"56","author":"Yim","year":"2021","journal-title":"Dev. Cell"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1146\/annurev-cellbio-092910-154005","article-title":"The role of Atg proteins in autophagosome formation","volume":"27","author":"Mizushima","year":"2011","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1038\/cr.2013.169","article-title":"Historical landmarks of autophagy research","volume":"24","author":"Ohsumi","year":"2014","journal-title":"Cell Res."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1038\/s41580-018-0003-4","article-title":"Mechanism and medical implications of mammalian autophagy","volume":"19","author":"Dikic","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Kirchner, P., Bourdenx, M., Madrigal-Matute, J., Tiano, S., Diaz, A., Bartholdy, B.A., Will, B., and Cuervo, A.M. (2019). Proteome-wide analysis of chaperone-mediated autophagy targeting motifs. PLoS Biol., 17.","DOI":"10.1371\/journal.pbio.3000301"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1937","DOI":"10.4161\/auto.26448","article-title":"HSPA8\/HSC70 chaperone protein: Structure, function, and chemical targeting","volume":"9","author":"Stricher","year":"2013","journal-title":"Autophagy"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1038\/s41580-018-0001-6","article-title":"The coming of age of chaperone-mediated autophagy","volume":"19","author":"Kaushik","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1984","DOI":"10.1080\/15548627.2016.1208887","article-title":"Selective endosomal microautophagy is starvation-inducible in Drosophila","volume":"12","author":"Mukherjee","year":"2016","journal-title":"Autophagy"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"673","DOI":"10.4161\/auto.7.7.14733","article-title":"Microautophagy in mammalian cells: Revisiting a 40-year-old conundrum","volume":"7","author":"Mijaljica","year":"2011","journal-title":"Autophagy"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1016\/j.exphem.2011.01.008","article-title":"Quiescence regulators for hematopoietic stem cell","volume":"39","author":"Li","year":"2011","journal-title":"Exp. Hematol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"4936","DOI":"10.1158\/1078-0432.CCR-10-1499","article-title":"Stem cell quiescence","volume":"17","author":"Li","year":"2011","journal-title":"Clin. Cancer Res."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1126\/science.aag3048","article-title":"Lysosome activation clears aggregates and enhances quiescent neural stem cell activation during aging","volume":"359","author":"Leeman","year":"2018","journal-title":"Science"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"5446","DOI":"10.1038\/s41467-019-13203-4","article-title":"Enhanced lysosomal degradation maintains the quiescent state of neural stem cells","volume":"10","author":"Kobayashi","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"3082","DOI":"10.1111\/febs.15555","article-title":"Lysosomes and signaling pathways for maintenance of quiescence in adult neural stem cells","volume":"288","author":"Kobayashi","year":"2021","journal-title":"FEBS J."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"22624","DOI":"10.1073\/pnas.1915905116","article-title":"Graded regulation of cellular quiescence depth between proliferation and senescence by a lysosomal dimmer switch","volume":"116","author":"Fujimaki","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.stem.2018.11.021","article-title":"Lysosomal Signaling Licenses Embryonic Stem Cell Differentiation via Inactivation of Tfe3","volume":"24","author":"Villegas","year":"2018","journal-title":"Cell Stem Cell"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"3623","DOI":"10.1038\/s41467-019-11568-0","article-title":"MYC competes with MiT\/TFE in regulating lysosomal biogenesis and autophagy through an epigenetic rheostat","volume":"10","author":"Annunziata","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1101\/gad.274142.115","article-title":"AMPK governs lineage specification through Tfeb-dependent regulation of lysosomes","volume":"30","author":"Young","year":"2016","journal-title":"Genes Dev."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1007\/s11010-020-03978-2","article-title":"Autophagy: A promising therapeutic target for improving mesenchymal stem cell biological functions","volume":"476","author":"Deng","year":"2021","journal-title":"Mol. Cell. Biochem."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/j.stem.2020.01.013","article-title":"Restraining Lysosomal Activity Preserves Hematopoietic Stem Cell Quiescence and Potency","volume":"26","author":"Liang","year":"2020","journal-title":"Cell Stem Cell"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"4206","DOI":"10.1242\/dev.107086","article-title":"Stem cells and the impact of ROS signaling","volume":"141","author":"Bigarella","year":"2014","journal-title":"Development"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1038\/ncb3385","article-title":"Metabolic regulation of stem cell function in tissue homeostasis and organismal ageing","volume":"18","author":"Chandel","year":"2016","journal-title":"Nat. Cell Biol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1182\/bloodadvances.2020003658","article-title":"Using mitochondrial activity to select for potent human hematopoietic stem cells","volume":"5","author":"Qiu","year":"2021","journal-title":"Blood Adv."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1016\/j.stem.2021.02.017","article-title":"Lysosomal Regulation of Metabolism in Quiescent Hematopoietic Stem Cells: More than Just Autophagy","volume":"28","author":"Ghaffari","year":"2021","journal-title":"Cell Stem Cell"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1038\/nature21388","article-title":"Autophagy maintains the metabolism and function of young and old stem cells","volume":"543","author":"Ho","year":"2017","journal-title":"Nature"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1111\/nyas.14284","article-title":"Pitfalls and requirements in quantifying asymmetric mitotic segregation","volume":"1466","author":"Loeffler","year":"2020","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.stem.2020.01.016","article-title":"Asymmetrically Segregated Mitochondria Provide Cellular Memory of Hematopoietic Stem Cell Replicative History and Drive HSC Attrition","volume":"26","author":"Hinge","year":"2020","journal-title":"Cell Stem Cell"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1097\/MOH.0000000000000644","article-title":"Symmetric and asymmetric activation of hematopoietic stem cells","volume":"28","author":"Loeffler","year":"2021","journal-title":"Curr. Opin. Hematol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1838","DOI":"10.1016\/j.stem.2021.07.003","article-title":"TFEB-mediated endolysosomal activity controls human hematopoietic stem cell fate","volume":"28","author":"Kaufmann","year":"2021","journal-title":"Cell Stem Cell"},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Tazhitdinova, R., and Timoshenko, A.V. (2020). The Emerging Role of Galectins and O-GlcNAc Homeostasis in Processes of Cellular Differentiation. Cells, 9.","DOI":"10.3390\/cells9081792"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"2118","DOI":"10.1038\/s41467-021-22346-2","article-title":"Indispensable role of Galectin-3 in promoting quiescence of hematopoietic stem cells","volume":"12","author":"Jia","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1594","DOI":"10.1182\/bloodadvances.2020002410","article-title":"Autophagy is dispensable for the maintenance of hematopoietic stem cells in neonates","volume":"5","author":"Hashimoto","year":"2021","journal-title":"Blood Adv."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1038\/nature11895","article-title":"FOXO3A directs a protective autophagy program in haematopoietic stem cells","volume":"494","author":"Warr","year":"2013","journal-title":"Nature"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1084\/jem.20101145","article-title":"The autophagy protein Atg7 is essential for hematopoietic stem cell maintenance","volume":"208","author":"Mortensen","year":"2011","journal-title":"J. Exp. Med."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.4161\/auto.7.9.15886","article-title":"Lack of autophagy in the hematopoietic system leads to loss of hematopoietic stem cell function and dysregulated myeloid proliferation","volume":"7","author":"Mortensen","year":"2011","journal-title":"Autophagy"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"1719","DOI":"10.4161\/cc.10.11.15673","article-title":"Autophagy in the pathogenesis of myelodysplastic syndrome and acute myeloid leukemia","volume":"10","author":"Watson","year":"2011","journal-title":"Cell Cycle"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"15008","DOI":"10.1038\/cddiscovery.2015.8","article-title":"Autophagy limits proliferation and glycolytic metabolism in acute myeloid leukemia","volume":"1","author":"Watson","year":"2015","journal-title":"Cell Death Discov."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"4806","DOI":"10.1182\/blood-2010-06-288589","article-title":"FIP200 is required for the cell-autonomous maintenance of fetal hematopoietic stem cells","volume":"116","author":"Liu","year":"2010","journal-title":"Blood"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"e12","DOI":"10.4110\/in.2019.19.e12","article-title":"The autophagy Protein Atg5 Plays a Crucial Role in the Maintenance and Reconstitution Ability of Hematopoietic Stem Cells","volume":"19","author":"Jung","year":"2019","journal-title":"Immune Netw."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1038\/s41586-020-03129-z","article-title":"Chaperone-mediated autophagy sustains haematopoietic stem-cell function","volume":"591","author":"Dong","year":"2021","journal-title":"Nature"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.cell.2018.09.048","article-title":"Biological Functions of Autophagy Genes: A Disease Perspective","volume":"176","author":"Levine","year":"2019","journal-title":"Cell"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1097\/BS9.0000000000000051","article-title":"BECN1 modulates hematopoietic stem cells by targeting Caspa-se-3-GSDME-mediated pyroptosis","volume":"2","author":"Yang","year":"2020","journal-title":"Blood Sci."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.1126\/science.aaf5530","article-title":"Self-renewal of a purified Tie2 + hematopoietic stem cell population relies on mitochondrial clearance","volume":"354","author":"Ito","year":"2016","journal-title":"Science"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1038\/s41590-017-0002-1","article-title":"Atad3a suppresses Pink1-dependent mitophagy to maintain homeostasis of hematopoietic progenitor cells","volume":"19","author":"Jin","year":"2017","journal-title":"Nat. Immunol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"2522","DOI":"10.1038\/s41467-021-22749-1","article-title":"MAEA is an E3 ubiquitin ligase promoting autophagy and maintenance of haematopoietic stem cells","volume":"12","author":"Wei","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/S1476-5586(03)80037-4","article-title":"Extracellular acidification alters lysosomal trafficking in human breast cancer cells","volume":"5","author":"Glunde","year":"2003","journal-title":"Neoplasia"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1146\/annurev-pharmtox-010715-103101","article-title":"Critical Functions of the Lysosome in Cancer Biology","volume":"57","author":"Davidson","year":"2017","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"e1500603","DOI":"10.1126\/sciadv.1500603","article-title":"Regulated lysosomal exocytosis mediates cancer progression","volume":"1","author":"Machado","year":"2015","journal-title":"Sci. Adv."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1038\/s41419-018-1227-0","article-title":"Lysosomotropic drugs activate TFEB via lysosomal membrane fluidization and consequent inhibition of mTORC1 activity","volume":"9","author":"Zhitomirsky","year":"2018","journal-title":"Cell Death Dis."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"E8479","DOI":"10.1073\/pnas.1706526115","article-title":"Metastatic cells are preferentially vulnerable to lysosomal inhibition","volume":"115","author":"Morgan","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1038\/s41573-019-0036-1","article-title":"Lysosomes as a therapeutic target","volume":"18","author":"Bonam","year":"2019","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"e202102001","DOI":"10.1083\/jcb.202102001","article-title":"Lysosome biogenesis: Regulation and functions","volume":"220","author":"Yang","year":"2021","journal-title":"J. Cell Biol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"9801","DOI":"10.1007\/s11033-020-05993-4","article-title":"Endosomes, lysosomes, and the role of endosomal and lysosomal biogenesis in cancer development","volume":"47","author":"Jeger","year":"2020","journal-title":"Mol. Biol. Rep."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"6051","DOI":"10.1073\/pnas.0931430100","article-title":"Cloning of an Alpha-TFEB fusion in renal tumors harboring the t(6;11)(p21;q13) chromosome translocation","volume":"100","author":"Davis","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.1093\/hmg\/ddg178","article-title":"Upregulation of the transcription factor TFEB in t(6;11)(p21;q13)-positive renal cell carcinomas due to promoter substitution","volume":"12","author":"Kuiper","year":"2003","journal-title":"Hum. Mol. Genet."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1158\/2643-3230.BCD-20-0029","article-title":"TFEB Links MYC signaling to epigenetic control of myeloid differentiation and acute myeloid leukemia","volume":"2","author":"Yun","year":"2021","journal-title":"Blood Cancer Discov."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1182\/blood.V5.9.847.847","article-title":"Microscopic and histochemical studies on the Auer bodies in leukemic cells","volume":"5","author":"Ackerman","year":"1950","journal-title":"Blood"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1016\/j.leukres.2008.09.014","article-title":"John Auer and Auer rods; controversies revisited","volume":"33","author":"Yoshida","year":"2009","journal-title":"Leuk. Res."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.coi.2018.12.004","article-title":"The labyrinth unfolds: Architectural rearrangements of the endolysosomal system in antigen-presenting cells","volume":"58","author":"Perrin","year":"2019","journal-title":"Curr. Opin. Immunol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1093\/labmed\/lmaa027","article-title":"Autophagy in Hematological Malignancies: Molecular Aspects in Leukemia and Lymphoma","volume":"52","author":"Boustani","year":"2021","journal-title":"Lab. Med."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"1482795","DOI":"10.1155\/2018\/1482795","article-title":"Low Autophagy (ATG) Gene Expression Is Associated with an Immature AML Blast Cell Phenotype and Can Be Restored during AML Differentiation Therapy","volume":"2018","author":"Jin","year":"2018","journal-title":"Oxidative Med. Cell. Longev."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1182\/blood-2011-02-336487","article-title":"MiR-17\/20\/93\/106 promote hematopoietic cell expansion by targeting sequestosome 1\u2013regulated pathways in mice","volume":"118","author":"Meenhuis","year":"2011","journal-title":"Blood"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"e970066","DOI":"10.4161\/23723548.2014.970066","article-title":"Pro-survival role of p62 during granulocytic differentiation of acute myeloid leukemia cells","volume":"1","author":"Tschan","year":"2014","journal-title":"Mol. Cell. Oncol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1182\/blood-2018-02-833475","article-title":"Loss of the selective autophagy receptor p62 impairs murine myeloid leukemia progression and mitophagy","volume":"133","author":"Nguyen","year":"2019","journal-title":"Blood"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"e2361","DOI":"10.1038\/cddis.2016.264","article-title":"Atg5-dependent autophagy contributes to the development of acute myeloid leukemia in an MLL-AF9-driven mouse model","volume":"7","author":"Liu","year":"2016","journal-title":"Cell Death Dis."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1614","DOI":"10.1182\/blood-2015-12-684696","article-title":"Cytoprotective autophagy maintains leukemia-initiating cells in murine myeloid leukemia","volume":"128","author":"Sumitomo","year":"2016","journal-title":"Blood"},{"key":"ref_149","doi-asserted-by":"crossref","unstructured":"Joffre, C., Ducau, C., Poillet-Perez, L., Courdy, C., and Mas, V.M.-D. (2021). Autophagy a Close Relative of AML Biology. Biology, 10.","DOI":"10.3390\/biology10060552"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"2189","DOI":"10.1038\/s41375-018-0102-4","article-title":"RET-mediated autophagy suppression as targetable co-dependence in acute myeloid leukemia","volume":"32","author":"Rudat","year":"2018","journal-title":"Leukemia"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1038\/onc.2017.376","article-title":"Oncogenic FLT3-ITD supports autophagy via ATF4 in acute myeloid leukemia","volume":"37","author":"Heydt","year":"2017","journal-title":"Oncogene"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"2289","DOI":"10.7150\/thno.19439","article-title":"NPM1 Mutant Mediated PML Delocalization and Stabilization Enhances Autophagy and Cell Survival in Leukemic Cells","volume":"7","author":"Zou","year":"2017","journal-title":"Theranostics"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"3090","DOI":"10.1038\/s41467-018-05311-4","article-title":"A metabolic interplay coordinated by HLX regulates myeloid differentiation and AML through partly overlapping pathways","volume":"9","author":"Piragyte","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1172\/JCI64180","article-title":"Lysosomal disruption preferentially targets acute myeloid leukemia cells and progenitors","volume":"123","author":"Sukhai","year":"2013","journal-title":"J. Clin. Investig."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/j.ccr.2013.08.003","article-title":"Transformation-associated changes in sphingolipid metabolism sensitize cells to lysosomal cell death induced by inhibitors of acid sphingomyelinase","volume":"24","author":"Petersen","year":"2013","journal-title":"Cancer Cell"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"31761","DOI":"10.1074\/jbc.M113.514091","article-title":"P-glycoprotein mediates drug resistance via a novel mechanism involving lysosomal sequestration","volume":"288","author":"Yamagishi","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"2217","DOI":"10.1158\/0008-5472.CAN-06-3520","article-title":"Vincristine Induces Dramatic Lysosomal Changes and Sensitizes Cancer Cells to Lysosome-Destabilizing Siramesine","volume":"67","author":"Ostenfeld","year":"2007","journal-title":"Cancer Res."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/j.ebiom.2019.08.021","article-title":"Dual lysosomal-mitochondrial targeting by antihistamines to eradicate leukaemic cells","volume":"47","author":"Torrente","year":"2019","journal-title":"EBioMedicine"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"4841","DOI":"10.18632\/oncotarget.6739","article-title":"PIG7 promotes leukemia cell chemosensitivity via lysosomal membrane permeabilization","volume":"7","author":"Liu","year":"2016","journal-title":"Oncotarget"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.canlet.2009.02.023","article-title":"Small interfering RNA targeting the subunit ATP6L of proton pump V-ATPase overcomes chemoresistance of breast cancer cells","volume":"280","author":"You","year":"2009","journal-title":"Cancer Lett."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"948","DOI":"10.1007\/s10495-015-1123-3","article-title":"Select microtubule inhibitors increase lysosome acidity and promote lysosomal disruption in acute myeloid leukemia (AML) cells","volume":"20","author":"Bernard","year":"2015","journal-title":"Apoptosis"},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"43508","DOI":"10.18632\/oncotarget.6180","article-title":"Anti-leukemic effects of the V-ATPase inhibitor Archazolid A","volume":"6","author":"Zhang","year":"2015","journal-title":"Oncotarget"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1007\/s11306-020-01710-1","article-title":"Cationic amphiphilic drugs induce elevation in lysoglycerophospholipid levels and cell death in leukemia cells","volume":"16","author":"Nielsen","year":"2020","journal-title":"Metabolomics"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1080\/01635581.2020.1752745","article-title":"Quercetin Triggers Induction of Apoptotic and Lysosomal Death of Sensitive and Multidrug Resistant Leukaemia HL60 Cells","volume":"73","author":"Maruszewska","year":"2020","journal-title":"Nutr. Cancer"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"5871","DOI":"10.1158\/0008-5472.CAN-11-1218","article-title":"Antitumor activity of metal-chelating compound Dp44mT is mediated by formation of a Redox-active copper complex that accumulates in lysosomes","volume":"71","author":"Lovejoy","year":"2011","journal-title":"Cancer Res."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"e2510","DOI":"10.1038\/cddis.2016.381","article-title":"A mechanism for overcoming P-glycoprotein-mediated drug resistance: Novel combination therapy that releases stored doxorubicin from lysosomes via lysosomal permeabilization using Dp44mT or DpC","volume":"7","author":"Seebacher","year":"2016","journal-title":"Cell Death Dis."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"1450","DOI":"10.1182\/blood-2004-03-0868","article-title":"Novel di-2-pyridyl\u2013derived iron chelators with marked and selective antitumor activity: In vitro and in vivo assessment","volume":"104","author":"Yuan","year":"2004","journal-title":"Blood"},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.exphem.2017.02.004","article-title":"Role of mTORC1\u2013S6K1 signaling pathway in regulation of hematopoietic stem cell and acute myeloid leukemia","volume":"50","author":"Ghosh","year":"2017","journal-title":"Exp. Hematol."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1007\/s12185-019-02701-2","article-title":"An mTORC1\/2 dual inhibitor, AZD2014, acts as a lysosomal function activator and enhances gemtuzumab ozogamicin-induced apoptosis in primary human leukemia cells","volume":"110","author":"Mizutani","year":"2019","journal-title":"Int. J. Hematol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"2114","DOI":"10.1172\/JCI62279","article-title":"mTORC1 is essential for leukemia propagation but not stem cell self-renewal","volume":"122","author":"Hoshii","year":"2012","journal-title":"J. Clin. Investig."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"1266","DOI":"10.1038\/s41375-019-0659-6","article-title":"Pre-clinical activity of combined LSD1 and mTORC1 inhibition in MLL-translocated acute myeloid leukaemia","volume":"34","author":"Deb","year":"2020","journal-title":"Leukemia"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"2795","DOI":"10.1158\/1078-0432.CCR-18-1474","article-title":"Activation of the Lysosome-Associated Membrane Protein LAMP5 by DOT1L Serves as a Bodyguard for MLL Fusion Oncoproteins to Evade Degradation in Leukemia","volume":"25","author":"Wang","year":"2019","journal-title":"Clin. Cancer Res."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"144889","DOI":"10.1016\/j.gene.2020.144889","article-title":"Targeting ferroptosis contributes to ATPR-induced AML differentiation via ROS-autophagy-lysosomal pathway","volume":"755","author":"Du","year":"2020","journal-title":"Gene"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"2465","DOI":"10.1038\/s41418-021-00768-1","article-title":"Reducing FASN expression sensitizes acute myeloid leukemia cells to differentiation therapy","volume":"28","author":"Humbert","year":"2021","journal-title":"Cell Death Differ."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"101159","DOI":"10.1016\/j.tranon.2021.101159","article-title":"Targeting IFN-\u03b3-inducible lysosomal thiol reductase overcomes chemoresistance in AML through regulating the ROS-mediated mitochondrial damage","volume":"14","author":"Niu","year":"2021","journal-title":"Transl. Oncol."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1038\/nrc4027","article-title":"Cysteine cathepsin proteases: Regulators of cancer progression and therapeutic response","volume":"15","author":"Olson","year":"2015","journal-title":"Nat. Rev. Cancer"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pharmthera.2019.02.003","article-title":"Cathepsins: Potent regulators in carcinogenesis","volume":"198","author":"Khaket","year":"2019","journal-title":"Pharmacol. Ther."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"7709","DOI":"10.1002\/jcp.29710","article-title":"Prognostic role and therapeutic susceptibility of cathepsin in various types of solid tumor and leukemia: A systematic review","volume":"235","author":"Hadad","year":"2020","journal-title":"J. Cell. Physiol."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1186\/s13045-021-01087-1","article-title":"Role of lysosomes in physiological activities, diseases, and therapy","volume":"14","author":"Zhang","year":"2021","journal-title":"J. Hematol. Oncol."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"eaao0422","DOI":"10.1126\/scisignal.aao0422","article-title":"Abl and Arg mediate cysteine cathepsin secretion to facilitate melanoma invasion and metastasis","volume":"11","author":"Tripathi","year":"2018","journal-title":"Sci. Signal."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"2775","DOI":"10.1038\/s41598-017-01894-y","article-title":"Cathepsin S inhibition combines control of systemic and peripheral pathomechanisms of autoimmune tissue injury","volume":"7","author":"Tato","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/j.biochi.2019.05.002","article-title":"Cystatins in cancer progression: More than just cathepsin inhibitors","volume":"166","author":"Breznik","year":"2019","journal-title":"Biochimie"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.arr.2016.04.010","article-title":"Lysosomal cathepsins and their regulation in aging and neurodegeneration","volume":"32","author":"Stoka","year":"2016","journal-title":"Ageing Res. Rev."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"16314","DOI":"10.1073\/pnas.1903330116","article-title":"Functional selection of protease inhibitory antibodies","volume":"116","author":"Lopez","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.pharmthera.2015.08.007","article-title":"Cathepsin L targeting in cancer treatment","volume":"155","author":"Sudhan","year":"2015","journal-title":"Pharmacol. Ther."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"1310","DOI":"10.7150\/ijbs.32987","article-title":"CSN6 Promotes the Migration and Invasion of Cervical Cancer Cells by Inhibiting Autophagic Degradation of Cathepsin L.","volume":"15","author":"Mao","year":"2019","journal-title":"Int. J. Biol. Sci."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1038\/s41598-019-57172-6","article-title":"Somatostatin receptor mediated targeting of acute myeloid leukemia by photodynamic metal complexes for light induced apoptosis","volume":"10","author":"Vegi","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_188","doi-asserted-by":"crossref","unstructured":"Kim, S.-Y., Kim, H.J., Kim, H.J., and Kim, C.-H. (2020). Non-Thermal Plasma Induces Antileukemic Effect Through mTOR Ubiquitination. Cells, 9.","DOI":"10.3390\/cells9030595"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"2015","DOI":"10.1021\/acs.molpharmaceut.0c01243","article-title":"Evaluation of the Anticancer Activity of pH-Sensitive Polyketal Nanoparticles for Acute Myeloid Leukemia","volume":"18","author":"Rajagopal","year":"2021","journal-title":"Mol. Pharm."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1038\/s41589-018-0161-x","article-title":"HIP1R targets PD-L1 to lysosomal degradation to alter T cell\u2013mediated cytotoxicity","volume":"15","author":"Wang","year":"2018","journal-title":"Nat. Chem. Biol."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.ebiom.2019.01.054","article-title":"SA-49, a novel aloperine derivative, induces MITF-dependent lysosomal degradation of PD-L1","volume":"40","author":"Zhang","year":"2019","journal-title":"EBioMedicine"},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1038\/s41586-020-2229-5","article-title":"Autophagy Promotes Immune Evasion of Pancreatic Cancer by Degrading MHC-I","volume":"581","author":"Yamamoto","year":"2020","journal-title":"Nature"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1186\/s13046-019-1343-4","article-title":"TFEB-driven autophagy potentiates TGF-\u03b2 induced migration in pancreatic cancer cells","volume":"38","author":"He","year":"2019","journal-title":"J. Exp. Clin. Cancer Res."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"2270","DOI":"10.1038\/s41467-017-02332-3","article-title":"Small-molecule TFEB pathway agonists that ameliorate metabolic syndrome in mice and extend C. elegans lifespan","volume":"8","author":"Wang","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"103207","DOI":"10.1016\/j.ebiom.2020.103207","article-title":"Transcription factor EB regulates cardiovascular homeostasis","volume":"63","author":"Lu","year":"2021","journal-title":"EBioMedicine"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.tem.2019.09.007","article-title":"Pros and Cons of Chaperone-Mediated Autophagy in Cancer Biology","volume":"31","author":"Arias","year":"2020","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1038\/s41401-018-0166-8","article-title":"CID1067700, a late endosome GTPase Rab7 receptor antagonist, attenuates brain atrophy, improves neurologic deficits and inhibits reactive astrogliosis in rat ischemic stroke","volume":"40","author":"Qin","year":"2018","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1111\/cas.15204","article-title":"TAS-116 (pimitespib), a heat shock protein 90 inhibitor, shows efficacy in preclinical models of adult T-cell leukemia","volume":"113","author":"Ikebe","year":"2022","journal-title":"Cancer Sci."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"1601","DOI":"10.1111\/cas.12540","article-title":"Heat shock protein 90 inhibitor NVP-AUY 922 exerts potent activity against adult T-cell leukemia\u2013lymphoma cells","volume":"105","author":"Taniguchi","year":"2014","journal-title":"Cancer Sci."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.jbiotec.2019.12.008","article-title":"Encapsulation of daunorubicin into Saccharomyces cerevisiae-derived lysosome as drug delivery vehicles for acute myeloid leukemia (AML) treatment","volume":"308","author":"Choi","year":"2019","journal-title":"J. Biotechnol."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1021\/acsomega.1c04771","article-title":"Lysosome-Targeting Strategy Using Polypeptides and Chimeric Molecules","volume":"7","author":"Mondal","year":"2020","journal-title":"ACS Omega"},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"1254","DOI":"10.1002\/ajh.25620","article-title":"Maintenance therapy in AML: The past, the present and the future","volume":"94","author":"Molica","year":"2019","journal-title":"Am. J. Hematol."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1080\/10428194.2019.1672060","article-title":"The role of cladribine in acute myeloid leukemia: An old drug up to new tricks","volume":"61","author":"Molica","year":"2020","journal-title":"Leuk. Lymphoma"},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"5148","DOI":"10.1111\/febs.15326","article-title":"Intracellular cathepsin C levels determine sensitivity of cells to leucyl-leucine methyl ester-triggered apoptosis","volume":"287","author":"Kavcic","year":"2020","journal-title":"FEBS J."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"525","DOI":"10.18632\/oncotarget.491","article-title":"The Hsp90 inhibitor NVP-AUY922-AG inhibits NF-kappaB signaling, overcomes microenvironmental cytoprotection and is highly synergistic with fludarabine in primary CLL cells","volume":"3","author":"Walsby","year":"2012","journal-title":"Oncotarget"},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"19512","DOI":"10.1073\/pnas.0709443104","article-title":"Small molecule obatoclax (GX15-070) antagonizes MCL-1 and overcomes MCL-1-mediated resistance to apoptosis","volume":"104","author":"Nguyen","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"2171","DOI":"10.1182\/blood-2011-11-391037","article-title":"Experience with obatoclax mesylate (GX15-070), a small molecule pan-Bcl-2 family antagonist in patients with relapsed or refractory classical Hodgkin lymphoma","volume":"119","author":"Oki","year":"2012","journal-title":"Blood"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"285","DOI":"10.3816\/CLML.2010.n.059","article-title":"Phase II study of obatoclax mesylate (GX15-070), a small-molecule BCL-2 family antagonist, for patients with myelofibrosis","volume":"10","author":"Parikh","year":"2010","journal-title":"Clin. Lymphoma Myeloma Leuk."},{"key":"ref_209","doi-asserted-by":"crossref","unstructured":"Koltai, T. (2020). Targeting the pH Paradigm at the Bedside: A Practical Approach. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21239221"},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"5563","DOI":"10.1021\/jacs.5b02150","article-title":"Discovery of a Small-Molecule Probe for V-ATPase Function","volume":"137","author":"Aldrich","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"5879","DOI":"10.1016\/j.bmcl.2008.07.003","article-title":"Evaluating the potential of vacuolar ATPase inhibitors as anticancer agents and multigram synthesis of the potent salicylihalamide analog saliphenylhalamide","volume":"18","author":"Lebreton","year":"2008","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1038\/sj.bjp.0705812","article-title":"A novel inhibitor of vacuolar ATPase, FR167356, which can discriminate between osteoclast vacuolar ATPase and lysosomal vacuolar ATPase","volume":"142","author":"Niikura","year":"2004","journal-title":"Br. J. Pharmacol."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"1579","DOI":"10.1359\/JBMR.050517","article-title":"A vacuolar ATPase inhibitor, FR167356, prevents bone resorption in ovariectomized rats with high potency and specificity: Potential for clinical application","volume":"20","author":"Niikura","year":"2005","journal-title":"J. Bone Miner. Res."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"1768","DOI":"10.1182\/blood-2016-09-736892","article-title":"Identification of apilimod as a first-in-class PIKfyve kinase inhibitor for treatment of B-cell non-Hodgkin lymphoma","volume":"129","author":"Gayle","year":"2017","journal-title":"Blood"},{"key":"ref_215","doi-asserted-by":"crossref","unstructured":"Martin, S., Harper, C.B., May, L.M., Coulson, E.J., Meunier, F.A., and Osborne, S.L. (2013). Inhibition of PIKfyve by YM-201636 dysregulates autophagy and leads to apoptosis-independent neuronal cell death. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0060152"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"1830","DOI":"10.1136\/annrheumdis-2012-202460","article-title":"Lupuzor\/P140 peptide in patients with systemic lupus erythematosus: A randomised, double-blind, placebo-controlled phase IIb clinical trial","volume":"72","author":"Zimmer","year":"2013","journal-title":"Ann. Rheum. Dis."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"10832","DOI":"10.18632\/oncotarget.24396","article-title":"Humanin enhances the cellular response to stress by activation of chaperone-mediated autophagy","volume":"9","author":"Gong","year":"2018","journal-title":"Oncotarget"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1083\/jcb.201606095","article-title":"Humanin is an endogenous activator of chaperone-mediated autophagy","volume":"217","author":"Gong","year":"2018","journal-title":"J. Cell Biol."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1016\/j.devcel.2013.08.003","article-title":"A TRP channel in the lysosome regulates large particle phagocytosis via focal exocytosis","volume":"26","author":"Samie","year":"2013","journal-title":"Dev. Cell"},{"key":"ref_220","doi-asserted-by":"crossref","unstructured":"Tancini, B., Buratta, S., Delo, F., Sagini, K., Chiaradia, E., Pellegrino, R.M., Emiliani, C., and Urbanelli, L. (2020). Lysosomal Exocytosis: The Extracellular Role of an Intracellular Organelle. Membranes, 10.","DOI":"10.3390\/membranes10120406"},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"35769","DOI":"10.1074\/jbc.M113.511212","article-title":"Suppression of lysosome function induces autophagy via a feedback down-regulation of MTOR complex 1 (MTORC1) activity","volume":"288","author":"Li","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1084\/jem.174.4.881","article-title":"Ammonium chloride, an inhibitor of phagosome-lysosome fusion in macrophages, concurrently induces phagosome-endosome fusion, and opens a novel pathway: Studies of a pathogenic mycobacterium and a nonpathogenic yeast","volume":"174","author":"Hart","year":"1991","journal-title":"J. Exp. Med."},{"key":"ref_223","first-page":"326","article-title":"Monensin and chloroquine inhibit transfer to lysosomes of endocytosed macromolecules in cultured mouse peritoneal macrophages","volume":"49","author":"Stenseth","year":"1989","journal-title":"Eur. J. Cell Biol."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.bcmd.2013.04.005","article-title":"Miglustat therapy in type 1 Gaucher disease: Clinical and safety outcomes in a multicenter retrospective cohort study","volume":"51","author":"Kuter","year":"2013","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1186\/s13023-016-0413-3","article-title":"Biochemical response to substrate reduction therapy versus enzyme replacement therapy in Gaucher disease type 1 patients","volume":"11","author":"Smid","year":"2016","journal-title":"Orphanet. J. Rare. Dis."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1186\/s13023-017-0565-9","article-title":"Lucerastat, an iminosugar with potential as substrate reduction therapy for glycolipid storage disorders: Safety, tolerability, and pharmacokinetics in healthy subjects","volume":"12","author":"Guerard","year":"2017","journal-title":"Orphanet. J. Rare. Dis."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1002\/cpt.790","article-title":"Lucerastat, an Iminosugar for Substrate Reduction Therapy: Tolerability, Pharmacodynamics, and Pharmacokinetics in Patients with Fabry Disease on Enzyme Replacement","volume":"103","author":"Guerard","year":"2018","journal-title":"Clin. Pharmacol. Ther."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1038\/mt.2016.53","article-title":"CNS-accessible Inhibitor of Glucosylceramide Synthase for Substrate Reduction Therapy of Neuronopathic Gaucher Disease","volume":"24","author":"Marshall","year":"2016","journal-title":"Mol. Ther."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"17054","DOI":"10.1074\/jbc.M114.555300","article-title":"The phytoestrogen genistein modulates lysosomal metabolism and transcription factor EB (TFEB) activation","volume":"289","author":"Moskot","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/j.curtheres.2008.04.002","article-title":"Genistin-rich soy isoflavone extract in substrate reduction therapy for Sanfilippo syndrome: An open-label, pilot study in 10 pediatric patients","volume":"69","author":"Piotrowska","year":"2008","journal-title":"Curr. Ther. Res. Clin. Exp."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.ymgme.2021.07.008","article-title":"MPS VI associated ocular phenotypes in an MPS VI murine model and the therapeutic effects of odiparcil treatment","volume":"135","author":"Entchev","year":"2022","journal-title":"Mol. Genet. Metab."},{"key":"ref_232","doi-asserted-by":"crossref","unstructured":"Entchev, E., Jantzen, I., Masson, P., Bocart, S., Bournique, B., Luccarini, J.M., Bouchot, A., Lacombe, O., Junien, J.L., and Broqua, P. (2020). Odiparcil, a potential glycosaminoglycans clearance therapy in mucopolysaccharidosis VI-Evidence from in vitro and in vivo models. PLoS ONE, 15.","DOI":"10.1371\/journal.pone.0233032"},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1007\/s40265-019-01090-4","article-title":"Migalastat: A Review in Fabry Disease","volume":"79","author":"McCafferty","year":"2019","journal-title":"Drugs"},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"13813","DOI":"10.1073\/pnas.0605928103","article-title":"The iminosugar isofagomine increases the activity of N370S mutant acid beta-glucosidase in Gaucher fibroblasts by several mechanisms","volume":"103","author":"Steet","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"1385","DOI":"10.1038\/s41598-018-19479-8","article-title":"Effects of ambroxol on the autophagy-lysosome pathway and mitochondria in primary cortical neurons","volume":"8","author":"Magalhaes","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"15912","DOI":"10.1073\/pnas.2536657100","article-title":"Chemical chaperone therapy for brain pathology in G(M1)-gangliosidosis","volume":"100","author":"Matsuda","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"2201","DOI":"10.1038\/mt.2012.152","article-title":"Pharmacological enhancement of alpha-glucosidase by the allosteric chaperone N-acetylcysteine","volume":"20","author":"Porto","year":"2012","journal-title":"Mol. Ther."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"7546","DOI":"10.1021\/jm3005543","article-title":"Discovery of a novel noniminosugar acid alpha glucosidase chaperone series","volume":"55","author":"Xiao","year":"2012","journal-title":"J. Med. Chem."},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1146\/annurev-med-122313-085916","article-title":"Lysosomal storage diseases: From pathophysiology to therapy","volume":"66","author":"Parenti","year":"2015","journal-title":"Annu. Rev. Med."},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1016\/j.ymgme.2014.05.009","article-title":"Pharmacological chaperones increase residual beta-galactocerebrosidase activity in fibroblasts from Krabbe patients","volume":"112","author":"Berardi","year":"2014","journal-title":"Mol. Genet. Metab."},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1038\/mt.2012.263","article-title":"A bicyclic 1-deoxygalactonojirimycin derivative as a novel pharmacological chaperone for GM1 gangliosidosis","volume":"21","author":"Takai","year":"2013","journal-title":"Mol. Ther."},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"7441","DOI":"10.1523\/JNEUROSCI.0636-16.2016","article-title":"A New Glucocerebrosidase Chaperone Reduces alpha-Synuclein and Glycolipid Levels in iPSC-Derived Dopaminergic Neurons from Patients with Gaucher Disease and Parkinsonism","volume":"36","author":"Aflaki","year":"2016","journal-title":"J. Neurosci."},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1016\/S0140-6736(18)30485-9","article-title":"Sirolimus in patients with clinically active systemic lupus erythematosus resistant to, or intolerant of, conventional medications: A single-arm, open-label, phase 1\/2 trial","volume":"391","author":"Lai","year":"2018","journal-title":"Lancet."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"5257","DOI":"10.3892\/mmr.2017.7285","article-title":"Modulation of the immune response in rheumatoid arthritis with strategically released rapamycin","volume":"16","author":"Shao","year":"2017","journal-title":"Mol. Med. Rep."},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1006\/bbrc.2001.4787","article-title":"Significance of cathepsin B accumulation in synovial fluid of rheumatoid arthritis","volume":"283","author":"Hashimoto","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1186\/1476-4598-9-207","article-title":"Cathepsin B inhibition interferes with metastatic potential of human melanoma: An in vitro and in vivo study","volume":"9","author":"Matarrese","year":"2010","journal-title":"Mol. Cancer."},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1007\/s00296-006-0210-8","article-title":"Cathepsin G: The significance in rheumatoid arthritis as a monocyte chemoattractant","volume":"27","author":"Miyata","year":"2007","journal-title":"Rheumatol. Int."},{"key":"ref_248","first-page":"61","article-title":"Cathepsins B and L in synovial fluids from patients with rheumatoid arthritis and the effect of cathepsin B on the activation of pro-urokinase","volume":"47","author":"Ikeda","year":"2000","journal-title":"J. Med. Investig."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1124\/mol.110.064261","article-title":"A small-molecule oxocarbazate inhibitor of human cathepsin L blocks severe acute respiratory syndrome and ebola pseudotype virus infection into human embryonic kidney 293T cells","volume":"78","author":"Shah","year":"2010","journal-title":"Mol. Pharmacol."},{"key":"ref_250","doi-asserted-by":"crossref","unstructured":"Yamada, A., Ishimaru, N., Arakaki, R., Katunuma, N., and Hayashi, Y. (2010). Cathepsin L inhibition prevents murine autoimmune diabetes via suppression of CD8(+) T cell activity. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0012894"},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1038\/nrm2258","article-title":"Melanosomes\u2014Dark organelles enlighten endosomal membrane transport","volume":"8","author":"Raposo","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1172\/JCI0214682","article-title":"Cathepsin S inhibitor prevents autoantigen presentation and autoimmunity","volume":"110","author":"Saegusa","year":"2002","journal-title":"J. Clin. Investig."},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.bbapap.2011.10.002","article-title":"Cysteine cathepsins: From structure, function and regulation to new frontiers","volume":"1824","author":"Turk","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1136\/annrheumdis-2013-203717","article-title":"Cathepsin S inhibition suppresses systemic lupus erythematosus and lupus nephritis because cathepsin S is essential for MHC class II-mediated CD4 T cell and B cell priming","volume":"74","author":"Rupanagudi","year":"2015","journal-title":"Ann. Rheum. Dis."},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1006\/bbrc.1999.1953","article-title":"Structure-based development of pyridoxal propionate derivatives as specific inhibitors of cathepsin K in vitro and in vivo","volume":"267","author":"Katunuma","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"1739","DOI":"10.1359\/jbmr.2001.16.10.1739","article-title":"Potent and selective inhibition of human cathepsin K leads to inhibition of bone resorption in vivo in a nonhuman primate","volume":"16","author":"Stroup","year":"2001","journal-title":"J. Bone Miner. Res."},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"920","DOI":"10.1021\/ml300197h","article-title":"Nonpeptidic lysosomal modulators derived from z-phe-ala-diazomethylketone for treating protein accumulation diseases","volume":"3","author":"Viswanathan","year":"2012","journal-title":"ACS Med. Chem. Lett."},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1186\/s13023-018-0844-0","article-title":"Miglustat in Niemann-Pick disease type C patients: A review","volume":"13","author":"Pineda","year":"2018","journal-title":"Orphanet. J. Rare Dis."}],"updated-by":[{"DOI":"10.3390\/cancers16132317","type":"retraction","label":"Retraction","source":"retraction-watch","updated":{"date-parts":[[2024,6,25]],"date-time":"2024-06-25T00:00:00Z","timestamp":1719273600000},"record-id":"66359"},{"DOI":"10.3390\/cancers16132317","type":"retraction","label":"Retraction","source":"publisher","updated":{"date-parts":[[2022,3,23]],"date-time":"2022-03-23T00:00:00Z","timestamp":1647993600000}}],"container-title":["Cancers"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6694\/14\/7\/1618\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,8,3]],"date-time":"2025-08-03T14:03:16Z","timestamp":1754229796000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6694\/14\/7\/1618"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,3,23]]},"references-count":258,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2022,4]]}},"alternative-id":["cancers14071618"],"URL":"https:\/\/doi.org\/10.3390\/cancers14071618","relation":{"retraction":[{"id-type":"doi","id":"10.3390\/cancers16132317","asserted-by":"object"}]},"ISSN":["2072-6694"],"issn-type":[{"value":"2072-6694","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,3,23]]}}}